node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
OJW04221.1 | OJW27912.1 | BGO49_31305 | BGO49_05830 | Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology. | ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.724 |
OJW12689.1 | OJW19649.1 | BGO49_25055 | BGO49_14370 | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.910 |
OJW12689.1 | OJW20965.1 | BGO49_25055 | BGO49_29870 | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.985 |
OJW12689.1 | OJW20966.1 | BGO49_25055 | BGO49_29875 | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.910 |
OJW12689.1 | OJW27912.1 | BGO49_25055 | BGO49_05830 | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.671 |
OJW12689.1 | nuoC | BGO49_25055 | BGO49_25045 | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. | 0.996 |
OJW12689.1 | nuoD | BGO49_25055 | BGO49_02390 | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. | 0.999 |
OJW19649.1 | OJW12689.1 | BGO49_14370 | BGO49_25055 | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.910 |
OJW19649.1 | OJW20965.1 | BGO49_14370 | BGO49_29870 | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | 0.999 |
OJW19649.1 | OJW20966.1 | BGO49_14370 | BGO49_29875 | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.814 |
OJW19649.1 | OJW27912.1 | BGO49_14370 | BGO49_05830 | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.580 |
OJW19649.1 | nuoC | BGO49_14370 | BGO49_25045 | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | NADH dehydrogenase; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 30 kDa subunit family. | 0.829 |
OJW19649.1 | nuoD | BGO49_14370 | BGO49_02390 | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | NADH-quinone oxidoreductase subunit B; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient; Belongs to the complex I 49 kDa subunit family. | 0.999 |
OJW20857.1 | OJW27912.1 | BGO49_29025 | BGO49_05830 | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UbiD family. | ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.740 |
OJW20857.1 | ubiX | BGO49_29025 | BGO49_05755 | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UbiD family. | 3-octaprenyl-4-hydroxybenzoate carboxy-lyase; Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN; Belongs to the UbiX/PAD1 family. | 0.987 |
OJW20965.1 | OJW12689.1 | BGO49_29870 | BGO49_25055 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | NAD(P)H-dependent oxidoreductase subunit E; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.985 |
OJW20965.1 | OJW19649.1 | BGO49_29870 | BGO49_14370 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c oxidase subunit I; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the heme-copper respiratory oxidase family. | 0.999 |
OJW20965.1 | OJW20966.1 | BGO49_29870 | BGO49_29875 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | Cytochrome c oxidase subunit I; Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. CO I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 and heme A of subunit 1 to the bimetallic center formed by heme A3 and copper B. | 0.999 |
OJW20965.1 | OJW24769.1 | BGO49_29870 | BGO49_06735 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | FAD-dependent oxidoreductase; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.634 |
OJW20965.1 | OJW27912.1 | BGO49_29870 | BGO49_05830 | Cytochrome c oxidase subunit II; Subunits I and II form the functional core of the enzyme complex. Electrons originating in cytochrome c are transferred via heme a and Cu(A) to the binuclear center formed by heme a3 and Cu(B). | ABC transporter; Derived by automated computational analysis using gene prediction method: Protein Homology. | 0.619 |